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A remote but significant sequence homology between glycoside hydrolase clan GH‐H and family GH31
Author(s) -
Janeček Štefan,
Svensson Birte,
MacGregor E. Ann
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.02.036
Subject(s) - clan , glycoside hydrolase , phylogenetic tree , biology , sequence (biology) , alpha (finance) , hydrolase , sequence homology , homology (biology) , peptide sequence , genetics , stereochemistry , chemistry , biochemistry , enzyme , gene , medicine , surgery , sociology , anthropology , construct validity , patient satisfaction
Although both the α‐amylase super‐family, i.e. the glycoside hydrolase (GH) clan GH‐H (the GH families 13, 70 and 77), and family GH31 share some characteristics, their different catalytic machinery prevents classification of GH31 in clan GH‐H. A significant but remote evolutionary relatedness is, however, proposed for clan GH‐H with GH31. A sequence alignment, based on the idea that residues equivalent in the primordial catalytic GH‐H/GH31 (β/α) 8 ‐barrel may not be found in the present‐day GH‐H and GH31 structures at strictly equivalent positions, shows remote sequence homologies covering β3, β4, β7 and β8 of the GH‐H and GH31 (β/α) 8 ‐barrels. Structure comparison of GH13 α‐amylase and GH31 α‐xylosidase guided alignment of GH‐H and GH31 members for construction of evolutionary trees. The closest sequence relationship displayed by GH31 is to GH77 of clan GH‐H.